Metabolic responsiveness to phorbol ester and activity of protein kinase C in isolated hepatocytes from partially hepatectomized rats

Biochem Biophys Res Commun. 1989 Jan 16;158(1):294-301. doi: 10.1016/s0006-291x(89)80211-6.

Abstract

The ability of isolated rat hepatocytes to respond to phorbol-12-myristate-13-acetate (PMA) with acute stimulation of de novo fatty acid synthesis was markedly depressed at 4, 22 and 48 h after partial hepatectomy (PH). This desensitization was not due to surgical stress as shown by comparison with hepatocytes from sham-operated animals. Moreover, the total activity of protein kinase C (PK-C), the principal phorbol ester receptor, was not down-regulated at 22 h after partial hepatectomy. Partial hepatectomy rather caused a small but distinct shift in subcellular PK-C distribution toward the particulate fraction thereby suggesting a modest activation of PK-C. We conclude that the PH-induced desensitization to PMA occurs at a point beyond PK-C activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyl-CoA Carboxylase / metabolism*
  • Animals
  • Cells, Cultured
  • DNA Replication
  • Fatty Acids / biosynthesis*
  • Hepatectomy
  • Ligases / metabolism*
  • Liver / drug effects
  • Liver / metabolism*
  • Liver Regeneration*
  • Male
  • Protein Kinase C / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Reference Values
  • Subcellular Fractions / enzymology
  • Tetradecanoylphorbol Acetate / pharmacology*

Substances

  • Fatty Acids
  • Protein Kinase C
  • Ligases
  • Acetyl-CoA Carboxylase
  • Tetradecanoylphorbol Acetate